The overall objective of this research is the understanding of the biological roles and mechanism of actions of a helix destabilizing protein (gene 32 protein) of bacteriophage T4 by analysis of its structure (and the structures of its complexes with other macromolecules such as nucleic acids or proteins). Two different types of the analysis are proposed; one is the biochemical analysis of 32 protein structure and the second is to contribute to the crystallographical analyses of Helix-Destabilizing Protein (HDP) and its derivatives. Biochemical analysis contains two interconnected lines of approach; one is to analyze the structure of modified proteins (mutational, chemical, proteolytic modifications) and correlate them to the altered activities and conformations of the modified proteins. The second line is mapping of contact area and detection of conformational changes in protein-nucleic acid or protein-protein complexes by differential chemical modification. Crystallographic approaches: There seems to be no doubt that the ultimate three dimensional structure of 32 protein (or its derivatives) has to be determined by crystallography and I intend to continue my contribution as a biochemist, to the crystallographic analyses of 32 protein. Two approaches are proposed. One is related to the electromicroscopic crystallography of 32 I-crystalline membrane and another is to make more crystal from 32 protein proteolysis fragments in forms different from what we already have.